RXA_XENLA
ID RXA_XENLA Reviewed; 322 AA.
AC O42201; B7ZRY4; O42566;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Retinal homeobox protein Rx-A;
DE Short=Rx1A;
DE Short=Xrx1;
DE AltName: Full=Retina and anterior neural fold homeobox protein A;
GN Name=rax-a; Synonyms=rx1, rx1a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Tail bud;
RX PubMed=9076688; DOI=10.1016/s0925-4773(96)00640-5;
RA Casarosa S., Andreazzoli M., Simeone A., Barsacchi G.;
RT "Xrx1, a novel Xenopus homeobox gene expressed during eye and pineal gland
RT development.";
RL Mech. Dev. 61:187-198(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ectoderm;
RX PubMed=9177348; DOI=10.1038/42475;
RA Mathers P.H., Grinberg A., Mahon K.A., Jamrich M.;
RT "The Rx homeobox gene is essential for vertebrate eye development.";
RL Nature 387:603-607(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a critical role in eye formation by regulating the
CC initial specification of retinal cells and/or their subsequent
CC proliferation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00138}.
CC -!- TISSUE SPECIFICITY: Highly expressed in anterior neural plate followed
CC by neural retina, pigmented epithelium, in pineal gland, diencephalon
CC floor and epiphysis. At later stages, the neuroretina remains the
CC primary site of expression. No expression in the developing lens and
CC cornea. {ECO:0000269|PubMed:9076688, ECO:0000269|PubMed:9177348}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in stage 11 (late-gastrula)
CC embryos and then appears to be maintained at fairly stable levels up to
CC stage 45 (late tadpole), when it declines.
CC {ECO:0000269|PubMed:9177348}.
CC -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF017273; AAB70267.1; -; mRNA.
DR EMBL; AF001048; AAB62322.1; -; mRNA.
DR EMBL; BC170331; AAI70331.1; -; mRNA.
DR EMBL; BC170333; AAI70333.1; -; mRNA.
DR RefSeq; NP_001081687.1; NM_001088218.1.
DR AlphaFoldDB; O42201; -.
DR SMR; O42201; -.
DR PRIDE; O42201; -.
DR GeneID; 397998; -.
DR KEGG; xla:397998; -.
DR CTD; 397998; -.
DR Xenbase; XB-GENE-6252134; rax.S.
DR OrthoDB; 1085093at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 397998; Expressed in camera-type eye and 2 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003654; OAR_dom.
DR InterPro; IPR043562; RAX/RAX2.
DR PANTHER; PTHR46271; PTHR46271; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03826; OAR; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50803; OAR; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..322
FT /note="Retinal homeobox protein Rx-A"
FT /id="PRO_0000049278"
FT DNA_BIND 130..189
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 75..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..39
FT /note="Octapeptide motif"
FT MOTIF 302..315
FT /note="OAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT MOTIF 308..312
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 75..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="T -> A (in Ref. 1; AAB70267)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="L -> S (in Ref. 1; AAB70267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36084 MW; 06B9BA6B8FA8EC97 CRC64;
MHLHSPSLMA DGSFSLSGHL LRSPGGNPSR LHSIEAILGF VKEDSVLGSF QSEISPRNAK
EVDKRSSRHC LHKMTEEIHP QQEHLEDGQT DGYGDPYLGK TSSECLSPGL STSNSDNKLS
DDEQQPKKKH RRNRTTFTTY QLHELERAFE KSHYPDVYSR EELAMKVNLP EVRVQVWFQN
RRAKWRRQEK LEVTSMKLQD SPMLSFNRSP QPSAMSALSS SLPLDSWLTP TLSNSTALQS
LPGFVTTPPS LPGSYTPPPF INPVSVGHAL QPLGAMGPPP PYQCGANFVD KYPLEETDPR
NNSIASLRMK AKEHIQFIGK PW
